ID W1DQL3_KLEPN Unreviewed; 230 AA.
AC W1DQL3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
OS Klebsiella pneumoniae IS43.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL11112.1, ECO:0000313|Proteomes:UP000019183};
RN [1] {ECO:0000313|EMBL:CDL11112.1, ECO:0000313|Proteomes:UP000019183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS43 {ECO:0000313|EMBL:CDL11112.1,
RC ECO:0000313|Proteomes:UP000019183};
RA Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT "Antibiotic resistance diversity of beta-lactamase producers in the General
RT Hospital Vienna.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL11112.1}.
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DR EMBL; CBWK010000607; CDL11112.1; -; Genomic_DNA.
DR AlphaFoldDB; W1DQL3; -.
DR eggNOG; COG0860; Bacteria.
DR Proteomes; UP000019183; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF2; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIA; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CDL11112.1}.
FT DOMAIN 59..214
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 230 AA; 25114 MW; 4960AB08D860ECB2 CRC64;
MLDPGHGGID TGAIGHNGSK EKHVVLAIAK NVRSILRSNG IDARLTRTGD TFIPLYDRVE
IAHQHGADLF MSIHADGFTN PSAAGASVFA LSNRGASSAM AKYLSDRENR ADEVAGKKAT
DKDHLLQQVL FDLVQTDTIK NSLTLGSHIL KKIKPVHKLH SRNTEQAAFV VLKSPSIPSV
LVETSFITNP NEEKLLGTTA FRQKIATAIA NGIISYFHWF DNQKAHSKRR
//
